Effect of an alpha-blocking agent, nicergoline, on the interaction between blood platelets, elastin and endothelial cells

Rafelson, Max E.; Migne, J; Santonja, R; Derouette, J.C.; Robert, L.

doi:10.1016/0006-2952(80)90225-7

Cited by 13 publications

(3 citation statements)

References 5 publications

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“…These results are in agreement with previous experiments using cPRP describing an inhibition by nicergoline of ADP-, collagen-J27, 28, 31], thrombin-, arachidonate-and A23187- [31] induced aggregation at concentrations from 100 to 700 /~M. Nicergoline is able to inhibit the adhesion of platelets to elastin [32] at 100 ~M and we report here that, at the same concentration, nicergoline inhibits the adhesion of washed platelets to a collagen-coated surface.…”

Section: Discussionsupporting

confidence: 95%

Potentiation by adrenaline of human platelet activation and the inhibition by the alpha-adrenergic antagonist nicergoline of platelet adhesion, secretion and aggregation

Lanza¹,

Cazenave²,

Beretz³

et al. 1986

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Adrenaline (1 to 10 microM) can induce the aggregation of human platelets suspended in citrated plasma but does not induce the aggregation of washed human platelets at doses as high as 1 mM, although these platelets respond normally to ADP, PAF-acether, collagen, arachidonic acid, thrombin, the endoperoxide analog U-46619 and the Ca2+ ionophore A23187. Adrenaline (0.5 microM) potentiates the aggregation and secretion induced by all the previous agonists in citrated platelet-rich plasma (cPRP) or in washed platelets. The activation by adrenaline of human platelets is mediated by alpha 2-adrenergic receptors, as demonstrated by inhibition with a series of adrenergic antagonists. The alpha-adrenergic antagonist nicergoline inhibits the activation of human platelets by adrenaline in the following situations: nicergoline inhibits the aggregation and secretion caused by adrenaline in cPRP (IC50 0.22 microM and 0.28 microM respectively); nicergoline inhibits the aggregation and secretion induced by the combination of adrenaline and each aggregating agent listed above in cPRP (IC50 ranging from 0.1 to 2.5 microM) or in washed platelets (IC50 ranging from 0.1 to 0.8 microM); nicergoline inhibits the binding of 3H-yohimbine to washed human platelets (IC50 0.26 microM); the intravenous administration of nicergoline (0.5 mg/kg per day) to patients inhibits significantly the ex vivo response of their platelets to adrenaline in cPRP. High concentrations of nicergoline also inhibit the aggregation and secretion induced by the aggregating agents listed above in cPRP (IC50 range 108 to 670 microM) and in washed platelets (IC50 range 27 to 140 microM) and the adhesion of platelets to collagen-coated surfaces. This latter effect is not mediated through blockade of alpha-adrenoceptors. A possible role of adrenaline in platelet activation in vivo could justify the use of nicergoline (Sermion), an alpha-adrenergic antagonist in combination therapy to prevent arterial thrombosis.

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Section: Discussionsupporting

confidence: 95%

Potentiation by adrenaline of human platelet activation and the inhibition by the alpha-adrenergic antagonist nicergoline of platelet adhesion, secretion and aggregation

Lanza¹,

Cazenave²,

Beretz³

et al. 1986

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“…For this reason, we paid attention to inhibition of platelet aggregation. Ordinas et al 5 and Refelson et al 6 indicated that there is an unambiguous interaction between platelets and elastin fibers and Kabemba et al 7 found that the elastin layer of the vascular wall has an antithrombotic action. Moreover, Sekiya and Okuda8 reported that elastin peptides prepared from bovine ligamentum nuchae inhibit platelet aggregation induced by thrombin.…”

Section: Introductionmentioning

confidence: 99%

Elastin peptides prepared from piscine and mammalian elastic tissues inhibit collagen‐induced platelet aggregation and stimulate migration and proliferation of human skin fibroblasts

Sugawara

Ura

Nakaba³

et al. 2010

Journal of Peptide Science

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We obtained pure elastin peptides from bovine ligamentum nuchae, porcine aorta, and bonito bulbus arteriosus. The inhibitory activity of these elastin peptides on platelet aggregation induced by collagen and the migratory and proliferative responsivenesses of human skin fibroblasts to these elastin peptides were examined. All of bonito, bovine, and porcine elastin peptides found to inhibit platelet aggregation, but bonito elastin peptides showed a higher inhibitory activity than bovine and porcine elastin peptides did. All elastin peptides enhanced the proliferation of fibroblasts 3.5- to 4.5-fold at a concentration of 10 µg/ml. Bovine and porcine elastin peptides stimulated the migration of fibroblasts, with the optimal response occurring at 10(-1) µg/ml, while maximal response was at 10(2) µg/ml for bonito elastin peptides. Furthermore, pretreatment of fibroblasts by lactose depressed their ability to migrate in response to all elastin peptides, suggesting the involvement of elastin receptor in cell response. These results suggest that both mammalian and piscine elastin peptides can be applied as useful biomaterials in which elasticity, antithrombotic property, and the enhancement of cell migration and proliferation are required.

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“…In comparison to the controls with TBS, the inhibition of the maximum extent of aggregation averaged 23% (range 10-62%) for the 10 inhibited cases and 10% for all cases with elastin. In this connection, it is noteworthy that Ordinas et al [ 10] and Rafelson et al [ 12] observed an adhesion reaction between fibrous elastin and human blood platelets, but, like in the assay system used here, the effect of elastin was much weaker than the one observed with collagen.…”

Section: Resultsmentioning

confidence: 71%

Effect of Collagen-Like Substances (Clq, Acetylcholinesterase and Elastin) on Collagen-Induced Platelet Aggregation

Csákó¹,

Suba²,

Herp³

1982

Pathophysiol Haemos Thromb

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The effects of collagen-like proteins on platelets were studied in human platelet-rich plasmas. The Clq subcomponent of complement (human), acetylcholinesterase (electric eel), and elastin (bovine) had no platelet aggregating activity, despite compositional homolo-gies with collagen in terms of hydroxyproline, hydroxylysine, proline and glycine contents. Upon preincubation with platelets, acetylcholinesterase was incapable of preventing the platelet aggregation triggered by collagen, whereas elastin exerted a weak and inconsistent blocking action. In turn, native Clq strongly inhibited collagen-induced platelet aggregation and ‘aggregated’ Clq, obtained by ultracentrifugation of freeze-thawed monomeric Clq, had a potentiating effect. These findings confirm the highly specific character of the platelet action of Clq.

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Effect of an alpha-blocking agent, nicergoline, on the interaction between blood platelets, elastin and endothelial cells

Cited by 13 publications

References 5 publications

Potentiation by adrenaline of human platelet activation and the inhibition by the alpha-adrenergic antagonist nicergoline of platelet adhesion, secretion and aggregation

Potentiation by adrenaline of human platelet activation and the inhibition by the alpha-adrenergic antagonist nicergoline of platelet adhesion, secretion and aggregation

Elastin peptides prepared from piscine and mammalian elastic tissues inhibit collagen‐induced platelet aggregation and stimulate migration and proliferation of human skin fibroblasts

Effect of Collagen-Like Substances (Clq, Acetylcholinesterase and Elastin) on Collagen-Induced Platelet Aggregation

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